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Type III secretion systems harbored by several Gram-negative bacteria are often used to deliver host-modulating effectors into infected eukaryotic cells. About 20 core proteins are needed for assembly of a secretion apparatus. Several of these proteins are genetically and functionally conserved in type III secretion systems of bacteria associated with invertebrate or vertebrate hosts. In the Ysc family of type III secretion systems are two poorly characterized protein families, the YscX family and the YscY family. In the plasmid-encoded Ysc-Yop type III secretion system of human pathogenic  Yersinia  species, YscX is a secreted substrate while YscY is its non-secreted cognate chaperone. Critically, neither an  yscX  nor  yscY  null mutant of  Yersinia  is capable of type III secretion. In this study, we show that the genetic equivalents of these proteins produced as components of other type III secretion systems of  Pseudomonas aeruginosa  (PscX and PscY),  Aeromonas  species (AscX and AscY),  Vibrio  species (VscX and VscY), and  Photorhabdus luminescens  (SctX and SctY) all possess an ability to interact with its native cognate partner and also establish cross-reciprocal binding to non-cognate partners as judged by a yeast two-hybrid assay. Moreover, a yeast three-hybrid assay also revealed that these heterodimeric complexes could maintain an interaction with YscV family members, a core membrane component of all type III secretion systems. Despite maintaining these molecular interactions, only expression of the native  yscX  in the near full-length  yscX  deletion and native  yscY  in the near full-length  yscY  deletion were able to complement for their general substrate secretion defects. Hence, YscX and YscY must have co-evolved to confer an important function specifically critical for  Yersinia  type III secretion.

Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion